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Protein

Membrane-bound transcription factor site-2 protease

Gene

Mbtps2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Intramembrane proteolysis of sterol-regulatory element-binding proteins (SREBPs) within the first transmembrane segment thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Site-2 cleavage comes after site-1 cleavage which takes place in the lumenal loop (By similarity).By similarity

Catalytic activityi

Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi167 – 1671Zinc; catalyticPROSITE-ProRule annotation
Active sitei168 – 1681PROSITE-ProRule annotation
Metal bindingi171 – 1711Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-MMU-381033. ATF6-alpha activates chaperones.

Protein family/group databases

MEROPSiM50.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound transcription factor site-2 protease (EC:3.4.24.85)
Alternative name(s):
Endopeptidase S2P
Gene namesi
Name:Mbtps2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:2444506. Mbtps2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33CytoplasmicBy similarity
Transmembranei4 – 2421HelicalSequence analysisAdd
BLAST
Topological domaini25 – 7450LumenalBy similarityAdd
BLAST
Transmembranei75 – 9521HelicalSequence analysisAdd
BLAST
Transmembranei96 – 10712HelicalSequence analysisAdd
BLAST
Topological domaini108 – 14033LumenalBy similarityAdd
BLAST
Transmembranei141 – 16525HelicalSequence analysisAdd
BLAST
Transmembranei170 – 18213HelicalSequence analysisAdd
BLAST
Transmembranei183 – 20523HelicalSequence analysisAdd
BLAST
Transmembranei225 – 24723HelicalSequence analysisAdd
BLAST
Topological domaini248 – 442195LumenalBy similarityAdd
BLAST
Transmembranei443 – 46018HelicalSequence analysisAdd
BLAST
Transmembranei461 – 47212HelicalSequence analysisAdd
BLAST
Topological domaini473 – 48816LumenalSequence analysisAdd
BLAST
Transmembranei489 – 50921HelicalSequence analysisAdd
BLAST
Topological domaini510 – 5156CytoplasmicSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Membrane-bound transcription factor site-2 proteasePRO_0000261592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8CHX6.
PaxDbiQ8CHX6.
PeptideAtlasiQ8CHX6.
PRIDEiQ8CHX6.

PTM databases

iPTMnetiQ8CHX6.
PhosphoSiteiQ8CHX6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000046873.
ExpressionAtlasiQ8CHX6. baseline and differential.
GenevisibleiQ8CHX6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059471.

Structurei

3D structure databases

ProteinModelPortaliQ8CHX6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi114 – 13219Poly-SerAdd
BLAST
Compositional biasi281 – 382102Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M50A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2921. Eukaryota.
COG0750. LUCA.
GeneTreeiENSGT00510000048066.
HOGENOMiHOG000231255.
HOVERGENiHBG006397.
InParanoidiQ8CHX6.
KOiK07765.
OMAiTELSHDH.
OrthoDBiEOG091G05YC.
TreeFamiTF314478.

Family and domain databases

InterProiIPR001193. MBTPS2.
IPR001478. PDZ.
IPR008915. Peptidase_M50.
[Graphical view]
PANTHERiPTHR13325. PTHR13325. 1 hit.
PfamiPF02163. Peptidase_M50. 1 hit.
[Graphical view]
PRINTSiPR01000. SREBPS2PTASE.
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CHX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPVSLLVVV VGGWTAVYLA DLVLKSSVYF KHSYEDWLEN NGLSISPFHI
60 70 80 90 100
RWQTSIFNRA FYSWGRRKAR MLYQWFNFGM VFGVIAMFSS FFLLGKTLMQ
110 120 130 140 150
TLAQMMADSP SPYSSSSSSS SSSSSSSSSS SSLHNEQVLQ VVVPGINLPV
160 170 180 190 200
NQLTYFFAAV LISGVVHEIG HGIAAIREQV RFNGFGIFLF IIYPGAFVDL
210 220 230 240 250
FTTHLQLISP VQQLRIFCAG IWHNFVLALL GILALVLLPV ILLPFYYTGV
260 270 280 290 300
GVLITEVAED SPAIGPRGLF VGDLVTHLQD CPVTNVQDWN ECLDTIAYEP
310 320 330 340 350
QIGYCISAST LQQLSFPVRA YKRLDGSTEC CNNHSLTDVC FSYRNNFNKR
360 370 380 390 400
LHTCLPARKA VEATQVCRSN KDCKSGASSS FCIVPSLETH TRLIKVKHPP
410 420 430 440 450
QIDMLYVGHP LHLHYTVSIT SFIPRFNFLS IDLPVIVETF VKYLISLSGA
460 470 480 490 500
LAIVNAVPCF ALDGQWILNS FLDATLTSVI GDNDVKDLIG FFILLGGSVL
510
LAANVTLGLW MVTAR
Length:515
Mass (Da):56,960
Last modified:March 1, 2003 - v1
Checksum:iE7C3A93A58D17A21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK148325 mRNA. Translation: BAE28482.1.
AK164486 mRNA. Translation: BAE37807.1.
AL663072 Genomic DNA. Translation: CAM18093.1.
BC038343 mRNA. Translation: AAH38343.1.
CCDSiCCDS30498.1.
RefSeqiNP_758511.1. NM_172307.3.
UniGeneiMm.37577.

Genome annotation databases

EnsembliENSMUST00000058098; ENSMUSP00000059471; ENSMUSG00000046873.
GeneIDi270669.
KEGGimmu:270669.
UCSCiuc009usb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK148325 mRNA. Translation: BAE28482.1.
AK164486 mRNA. Translation: BAE37807.1.
AL663072 Genomic DNA. Translation: CAM18093.1.
BC038343 mRNA. Translation: AAH38343.1.
CCDSiCCDS30498.1.
RefSeqiNP_758511.1. NM_172307.3.
UniGeneiMm.37577.

3D structure databases

ProteinModelPortaliQ8CHX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059471.

Protein family/group databases

MEROPSiM50.001.

PTM databases

iPTMnetiQ8CHX6.
PhosphoSiteiQ8CHX6.

Proteomic databases

MaxQBiQ8CHX6.
PaxDbiQ8CHX6.
PeptideAtlasiQ8CHX6.
PRIDEiQ8CHX6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058098; ENSMUSP00000059471; ENSMUSG00000046873.
GeneIDi270669.
KEGGimmu:270669.
UCSCiuc009usb.1. mouse.

Organism-specific databases

CTDi51360.
MGIiMGI:2444506. Mbtps2.

Phylogenomic databases

eggNOGiKOG2921. Eukaryota.
COG0750. LUCA.
GeneTreeiENSGT00510000048066.
HOGENOMiHOG000231255.
HOVERGENiHBG006397.
InParanoidiQ8CHX6.
KOiK07765.
OMAiTELSHDH.
OrthoDBiEOG091G05YC.
TreeFamiTF314478.

Enzyme and pathway databases

ReactomeiR-MMU-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-MMU-381033. ATF6-alpha activates chaperones.

Miscellaneous databases

ChiTaRSiMbtps2. mouse.
PROiQ8CHX6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000046873.
ExpressionAtlasiQ8CHX6. baseline and differential.
GenevisibleiQ8CHX6. MM.

Family and domain databases

InterProiIPR001193. MBTPS2.
IPR001478. PDZ.
IPR008915. Peptidase_M50.
[Graphical view]
PANTHERiPTHR13325. PTHR13325. 1 hit.
PfamiPF02163. Peptidase_M50. 1 hit.
[Graphical view]
PRINTSiPR01000. SREBPS2PTASE.
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMBTP2_MOUSE
AccessioniPrimary (citable) accession number: Q8CHX6
Secondary accession number(s): A2AC85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2003
Last modified: September 7, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.